From Malate Dehydrogenase to Phenyllactate Dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Substitution of S-(β-Aminoethyl)-Cysteine for Active-Site Lysine of Thermostable Aspartate Aminotransferase
2. Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine
3. Restoration of activity to catalytically deficient mutants of ribulosebisphosphate carboxylase/oxygenase by aminoethylation.
4. Regeneration of catalytic activity of glutamine synthetase mutants by chemical activation: Exploration of the role of arginines 339 and 359 in activity
5. Crystal structure of Escherichia coli malate dehydrogenase
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1. A Specialized Dehydrogenase Provides l ‐Phenyllactate for FR900359 Biosynthesis;ChemBioChem;2021-12-09
2. Heterologous Expression, Biosynthetic Studies, and Ecological Function of the Selective Gq‐Signaling Inhibitor FR900359;Angewandte Chemie International Edition;2018-01-15
3. Heterologe Expression, Biosynthese und ökologische Funktion des selektiven Gq‐Signaltransduktionsinhibitors FR900359;Angewandte Chemie;2017-12-20
4. In vitro Engineering of Novel Bioactivity in the Natural Enzymes;Frontiers in Chemistry;2016-10-07
5. Processing of N-Terminal Unnatural Amino Acids in Recombinant Human Interferon-β inEscherichia coli;ChemBioChem;2008-01-25
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